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Conserved domains on  [gi|446378603|ref|WP_000456458|]
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MULTISPECIES: peptide chain release factor N(5)-glutamine methyltransferase [Enterobacteriaceae]

Protein Classification

HemK/PrmC family methyltransferase( domain architecture ID 11483836)

HemK/PrmC family methyltransferase is a class I SAM-dependent methyltransferase that catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor; such as peptide chain release factor N(5)-glutamine methyltransferase that methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
1-275 9.77e-141

N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional


:

Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 396.84  E-value: 9.77e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603   1 MEYQHWLREAISQLQAsesPRRDAEILLEHVTGKGRTFILAFGETQLTDEQCQQLDALLTRRRDGEPIAHLTGVREFWSL 80
Cdd:PRK09328   2 MTIAEALREATARLAS---PRLDAELLLAHVLGLSRTDLLLNPEEELTPEELERFRALVARRAAGEPLQYILGEAEFWGL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603  81 PLFVSPATLIPRPDTECLVEQALARLP-EQPCRILDLGTGTGAIALALASERPDCEITAVDRMPDAVSLAQRNAQNLAIK 159
Cdd:PRK09328  79 DFKVSPGVLIPRPETEELVEWALEALLlKEPLRVLDLGTGSGAIALALAKERPDAEVTAVDISPEALAVARRNAKHGLGA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603 160 NIHILQSDWFSALAGQQFAMIVSNPPYIDEQDPHLQQGDVR-FEPLTALVAADSGMADIVHIIEQSRNALVSGGFLLLEH 238
Cdd:PRK09328 159 RVEFLQGDWFEPLPGGRFDLIVSNPPYIPEADIHLLQPEVRdHEPHLALFGGEDGLDFYRRIIEQAPRYLKPGGWLLLEI 238
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 446378603 239 GWQQGEAVRQAFIHAGYHDVETCRDYGDNERVTLGRY 275
Cdd:PRK09328 239 GYDQGEAVRALLAAAGFADVETRKDLAGRDRVVLGRR 275
 
Name Accession Description Interval E-value
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
1-275 9.77e-141

N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 396.84  E-value: 9.77e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603   1 MEYQHWLREAISQLQAsesPRRDAEILLEHVTGKGRTFILAFGETQLTDEQCQQLDALLTRRRDGEPIAHLTGVREFWSL 80
Cdd:PRK09328   2 MTIAEALREATARLAS---PRLDAELLLAHVLGLSRTDLLLNPEEELTPEELERFRALVARRAAGEPLQYILGEAEFWGL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603  81 PLFVSPATLIPRPDTECLVEQALARLP-EQPCRILDLGTGTGAIALALASERPDCEITAVDRMPDAVSLAQRNAQNLAIK 159
Cdd:PRK09328  79 DFKVSPGVLIPRPETEELVEWALEALLlKEPLRVLDLGTGSGAIALALAKERPDAEVTAVDISPEALAVARRNAKHGLGA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603 160 NIHILQSDWFSALAGQQFAMIVSNPPYIDEQDPHLQQGDVR-FEPLTALVAADSGMADIVHIIEQSRNALVSGGFLLLEH 238
Cdd:PRK09328 159 RVEFLQGDWFEPLPGGRFDLIVSNPPYIPEADIHLLQPEVRdHEPHLALFGGEDGLDFYRRIIEQAPRYLKPGGWLLLEI 238
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 446378603 239 GWQQGEAVRQAFIHAGYHDVETCRDYGDNERVTLGRY 275
Cdd:PRK09328 239 GYDQGEAVRALLAAAGFADVETRKDLAGRDRVVLGRR 275
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
1-277 8.35e-140

HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. Both E. coli and H. influenzae have two members rather than one. The members from the Mycoplasmas have an additional C-terminal domain. [Protein fate, Protein modification and repair]


Pssm-ID: 273125 [Multi-domain]  Cd Length: 284  Bit Score: 394.80  E-value: 8.35e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603    1 MEYQHWLREAISQLQASESPRRDAEILLEHVTGKGRTFILAFGETQLTDEQCQQLDALLTRRRDGEPIAHLTGVREFWSL 80
Cdd:TIGR00536   4 QEFLRWASSALSRAIARENPWLEALLLLEHDLGRERDLLLAFLTEELTPDEKERIFRLVLRRVKGVPVAYLLGSKEFYGL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603   81 PLFVSPATLIPRPDTECLVEQALARLPEQPC--RILDLGTGTGAIALALASERPDCEITAVDRMPDAVSLAQRNAQNLAI 158
Cdd:TIGR00536  84 EFFVNEHVLIPRPETEELVEKALASLISQPPilHILDLGTGSGCIALALAYEFPNAEVIAVDISPDALAVAEENAEKNQL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603  159 K-NIHILQSDWFSALAGQQFAMIVSNPPYIDEQDPHLQQGDVRFEPLTALVAADSGMADIVHIIEQSRNALVSGGFLLLE 237
Cdd:TIGR00536 164 EhRVEFIQSNLFEPLAGQKIDIIVSNPPYIDEEDLADLPNVVRFEPLLALVGGDDGLNILRQIIELAPDYLKPNGFLVCE 243
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 446378603  238 HG-WQQGEAVRQAFIHAGYHDVETCRDYGDNERVTLGRYYQ 277
Cdd:TIGR00536 244 IGnWQQKSLKELLRIKFTWYDVENGRDLNGKERVVLGFYHS 284
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
1-274 2.32e-133

Methylase of polypeptide chain release factors [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 378.34  E-value: 2.32e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603   1 MEYQHWLREAISQLQA--SESPRRDAEILLEHVTGKGRTFILAFGETQLTDEQCQQLDALLTRRRDGEPIAHLTGVREFW 78
Cdd:COG2890    1 MTIRELLRWAAARLAAagVDSARLEAELLLAHVLGLDRADLLLHPDRPLTEEELARLEALVARRAAGEPLAYILGEAEFY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603  79 SLPLFVSPATLIPRPDTECLVEQALARLP-EQPCRILDLGTGTGAIALALASERPDCEITAVDRMPDAVSLAQRNAQNLA 157
Cdd:COG2890   81 GLEFKVDPGVLIPRPETEELVELALALLPaGAPPRVLDLGTGSGAIALALAKERPDARVTAVDISPDALAVARRNAERLG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603 158 IKN-IHILQSDWFSALAG-QQFAMIVSNPPYIDEQDPHLQQGDVR-FEPLTALVAADSGMADIVHIIEQSRNALVSGGFL 234
Cdd:COG2890  161 LEDrVRFLQGDLFEPLPGdGRFDLIVSNPPYIPEDEIALLPPEVRdHEPRLALDGGEDGLDFYRRIIAQAPRLLKPGGWL 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 446378603 235 LLEHGWQQGEAVRQAFIHAGYHDVETCRDYGDNERVTLGR 274
Cdd:COG2890  241 LLEIGEDQGEAVRALLEAAGFADVETHKDLAGRDRVVVAR 280
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
112-236 8.37e-22

Methyltransferase small domain; This domain is found in ribosomal RNA small subunit methyltransferase C as well as other methyltransferases.


Pssm-ID: 428349 [Multi-domain]  Cd Length: 170  Bit Score: 89.19  E-value: 8.37e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603  112 RILDLGTGTGAIALALASERPDCEITAVDRMPDAVSLAQRNAQNLAIKNIHILQSDWFSALAGQQFAMIVSNPPYideqd 191
Cdd:pfam05175  34 KVLDLGCGAGVLGAALAKESPDAELTMVDINARALESARENLAANGLENGEVVASDVYSGVEDGKFDLIISNPPF----- 108
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 446378603  192 pHlQQGDVRFepltalvaadsgmaDIVH-IIEQSRNALVSGGFLLL 236
Cdd:pfam05175 109 -H-AGLATTY--------------NVAQrFIADAKRHLRPGGELWI 138
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
112-237 5.80e-17

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 74.39  E-value: 5.80e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603 112 RILDLGTGTGAIALALAsERPDCEITAVDRMPDAVSLAQRNAQNLAIKNIHILQSDWFSAL--AGQQFAMIVSNPPYide 189
Cdd:cd02440    1 RVLDLGCGTGALALALA-SGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPpeADESFDVIISDPPL--- 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 446378603 190 qdphlqqgdvrfepltalvaaDSGMADIVHIIEQSRNALVSGGFLLLE 237
Cdd:cd02440   77 ---------------------HHLVEDLARFLEEARRLLKPGGVLVLT 103
 
Name Accession Description Interval E-value
PRK09328 PRK09328
N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional
1-275 9.77e-141

N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional


Pssm-ID: 236467 [Multi-domain]  Cd Length: 275  Bit Score: 396.84  E-value: 9.77e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603   1 MEYQHWLREAISQLQAsesPRRDAEILLEHVTGKGRTFILAFGETQLTDEQCQQLDALLTRRRDGEPIAHLTGVREFWSL 80
Cdd:PRK09328   2 MTIAEALREATARLAS---PRLDAELLLAHVLGLSRTDLLLNPEEELTPEELERFRALVARRAAGEPLQYILGEAEFWGL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603  81 PLFVSPATLIPRPDTECLVEQALARLP-EQPCRILDLGTGTGAIALALASERPDCEITAVDRMPDAVSLAQRNAQNLAIK 159
Cdd:PRK09328  79 DFKVSPGVLIPRPETEELVEWALEALLlKEPLRVLDLGTGSGAIALALAKERPDAEVTAVDISPEALAVARRNAKHGLGA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603 160 NIHILQSDWFSALAGQQFAMIVSNPPYIDEQDPHLQQGDVR-FEPLTALVAADSGMADIVHIIEQSRNALVSGGFLLLEH 238
Cdd:PRK09328 159 RVEFLQGDWFEPLPGGRFDLIVSNPPYIPEADIHLLQPEVRdHEPHLALFGGEDGLDFYRRIIEQAPRYLKPGGWLLLEI 238
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 446378603 239 GWQQGEAVRQAFIHAGYHDVETCRDYGDNERVTLGRY 275
Cdd:PRK09328 239 GYDQGEAVRALLAAAGFADVETRKDLAGRDRVVLGRR 275
hemK_fam TIGR00536
HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme ...
1-277 8.35e-140

HemK family putative methylases; The gene hemK from E. coli was found to contribute to heme biosynthesis and originally suggested to be protoporphyrinogen oxidase. Functional analysis of the nearest homolog in Saccharomyces cerevisiae, YNL063w, finds it is not protoporphyrinogen oxidase and sequence analysis suggests that HemK homologs have S-adenosyl-methionine-dependent methyltransferase activity (Medline 99237242). Homologs are found, usually in a single copy, in nearly all completed genomes, but varying somewhat in apparent domain architecture. Both E. coli and H. influenzae have two members rather than one. The members from the Mycoplasmas have an additional C-terminal domain. [Protein fate, Protein modification and repair]


Pssm-ID: 273125 [Multi-domain]  Cd Length: 284  Bit Score: 394.80  E-value: 8.35e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603    1 MEYQHWLREAISQLQASESPRRDAEILLEHVTGKGRTFILAFGETQLTDEQCQQLDALLTRRRDGEPIAHLTGVREFWSL 80
Cdd:TIGR00536   4 QEFLRWASSALSRAIARENPWLEALLLLEHDLGRERDLLLAFLTEELTPDEKERIFRLVLRRVKGVPVAYLLGSKEFYGL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603   81 PLFVSPATLIPRPDTECLVEQALARLPEQPC--RILDLGTGTGAIALALASERPDCEITAVDRMPDAVSLAQRNAQNLAI 158
Cdd:TIGR00536  84 EFFVNEHVLIPRPETEELVEKALASLISQPPilHILDLGTGSGCIALALAYEFPNAEVIAVDISPDALAVAEENAEKNQL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603  159 K-NIHILQSDWFSALAGQQFAMIVSNPPYIDEQDPHLQQGDVRFEPLTALVAADSGMADIVHIIEQSRNALVSGGFLLLE 237
Cdd:TIGR00536 164 EhRVEFIQSNLFEPLAGQKIDIIVSNPPYIDEEDLADLPNVVRFEPLLALVGGDDGLNILRQIIELAPDYLKPNGFLVCE 243
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 446378603  238 HG-WQQGEAVRQAFIHAGYHDVETCRDYGDNERVTLGRYYQ 277
Cdd:TIGR00536 244 IGnWQQKSLKELLRIKFTWYDVENGRDLNGKERVVLGFYHS 284
HemK COG2890
Methylase of polypeptide chain release factors [Translation, ribosomal structure and ...
1-274 2.32e-133

Methylase of polypeptide chain release factors [Translation, ribosomal structure and biogenesis];


Pssm-ID: 442135 [Multi-domain]  Cd Length: 282  Bit Score: 378.34  E-value: 2.32e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603   1 MEYQHWLREAISQLQA--SESPRRDAEILLEHVTGKGRTFILAFGETQLTDEQCQQLDALLTRRRDGEPIAHLTGVREFW 78
Cdd:COG2890    1 MTIRELLRWAAARLAAagVDSARLEAELLLAHVLGLDRADLLLHPDRPLTEEELARLEALVARRAAGEPLAYILGEAEFY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603  79 SLPLFVSPATLIPRPDTECLVEQALARLP-EQPCRILDLGTGTGAIALALASERPDCEITAVDRMPDAVSLAQRNAQNLA 157
Cdd:COG2890   81 GLEFKVDPGVLIPRPETEELVELALALLPaGAPPRVLDLGTGSGAIALALAKERPDARVTAVDISPDALAVARRNAERLG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603 158 IKN-IHILQSDWFSALAG-QQFAMIVSNPPYIDEQDPHLQQGDVR-FEPLTALVAADSGMADIVHIIEQSRNALVSGGFL 234
Cdd:COG2890  161 LEDrVRFLQGDLFEPLPGdGRFDLIVSNPPYIPEDEIALLPPEVRdHEPRLALDGGEDGLDFYRRIIAQAPRLLKPGGWL 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 446378603 235 LLEHGWQQGEAVRQAFIHAGYHDVETCRDYGDNERVTLGR 274
Cdd:COG2890  241 LLEIGEDQGEAVRALLEAAGFADVETHKDLAGRDRVVVAR 280
RF_mod_PrmC TIGR03534
protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein ...
23-272 7.11e-133

protein-(glutamine-N5) methyltransferase, release factor-specific; Members of this protein family are HemK (PrmC), a protein once thought to be involved in heme biosynthesis but now recognized to be a protein-glutamine methyltransferase that modifies the peptide chain release factors. All members of the seed alignment are encoded next to the release factor 1 gene (prfA) and confirmed by phylogenetic analysis. SIMBAL analysis (manuscript in prep.) shows the motif [LIV]PRx[DE]TE (in Escherichia coli, IPRPDTE) confers specificity for the release factors rather than for ribosomal protein L3. [Protein fate, Protein modification and repair]


Pssm-ID: 274634 [Multi-domain]  Cd Length: 250  Bit Score: 376.04  E-value: 7.11e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603   23 DAEILLEHVTGKGRTFILAFGETQLTDEQCQQLDALLTRRRDGEPIAHLTGVREFWSLPLFVSPATLIPRPDTECLVEQA 102
Cdd:TIGR03534   1 DAELLLAHVLGKDRAQLLLHPEDELTPEELAAFDALLARRAAGEPVAYILGEREFYGLDFKVSPGVLIPRPETEELVEAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603  103 LARLPEQPcRILDLGTGTGAIALALASERPDCEITAVDRMPDAVSLAQRNAQNLAIKNIHILQSDWFSALAGQQFAMIVS 182
Cdd:TIGR03534  81 LERLKKGP-RVLDLGTGSGAIALALAKERPDARVTAVDISPEALAVARKNARRLGLENVEFLQGDWFEPLPSGKFDLIVS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603  183 NPPYIDEQDPHLQQGDVR-FEPLTALVAADSGMADIVHIIEQSRNALVSGGFLLLEHGWQQGEAVRQAFIHAGYHDVETC 261
Cdd:TIGR03534 160 NPPYIPEADIHLLDPEVRdFEPRLALFGGEDGLDFYRRIIAQAPRLLKPGGWLLLEIGYDQGEAVRALFEAAGFADVETR 239
                         250
                  ....*....|.
gi 446378603  262 RDYGDNERVTL 272
Cdd:TIGR03534 240 KDLAGKDRVVL 250
PRK14966 PRK14966
unknown domain/N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase fusion protein; ...
1-277 1.11e-64

unknown domain/N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase fusion protein; Provisional


Pssm-ID: 184930 [Multi-domain]  Cd Length: 423  Bit Score: 208.40  E-value: 1.11e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603   1 MEYQHWLreAISQLqasesPRRDAEILLEHVTGKGRTFILAFGETQLTDEQCQQLDALLTRRRDGEPIAHLTGVREFWSL 80
Cdd:PRK14966 151 MTFDEWL--GLSKL-----PKNEARMLLQYASEYTRVQLLTRGGEEMPDEVRQRADRLAQRRLNGEPVAYILGVREFYGR 223
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603  81 PLFVSPATLIPRPDTECLVEQALARLPEQPcRILDLGTGTGAIALALASERPDCEITAVDRMPDAVSLAQRNAQNLAIKn 160
Cdd:PRK14966 224 RFAVNPNVLIPRPETEHLVEAVLARLPENG-RVWDLGTGSGAVAVTVALERPDAFVRASDISPPALETARKNAADLGAR- 301
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603 161 IHILQSDWFSA--LAGQQFAMIVSNPPYIDEQDPHLQQGDVRFEPLTALVAADSGMADIVHIIEQSRNALVSGGFLLLEH 238
Cdd:PRK14966 302 VEFAHGSWFDTdmPSEGKWDIIVSNPPYIENGDKHLLQGDLRFEPQIALTDFSDGLSCIRTLAQGAPDRLAEGGFLLLEH 381
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 446378603 239 GWQQGEAVRQAFIHAGYHDVETCRDYGDNERVTLGRYYQ 277
Cdd:PRK14966 382 GFDQGAAVRGVLAENGFSGVETLPDLAGLDRVTLGKYMK 420
PRK01544 PRK01544
bifunctional N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase/tRNA (m7G46) ...
1-276 2.18e-47

bifunctional N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase/tRNA (m7G46) methyltransferase; Reviewed


Pssm-ID: 234958 [Multi-domain]  Cd Length: 506  Bit Score: 165.04  E-value: 2.18e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603   1 MEY--QHWLREAISQLQ--ASESPRRDAEILLEHVTGKGRTFILAFGETQLTDEQCQQLDALLTRRRDGEPIAHLTGVRE 76
Cdd:PRK01544   1 MQYsiKQILSDATDKLNkiGISSPQLEARILLQHVINKPIEYLLINLDEQLNEAEIEAFEKLLERRLKHEPIAYITGVKE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603  77 FWSLPLFVSPATLIPRPDTECLVEQAL-------------------------ARLPEQPCRILDLGTGTGAIALALASER 131
Cdd:PRK01544  81 FYSREFIVNKHVLIPRSDTEVLVDVVFqchsresgnpekkqlnpcfrgndisSNCNDKFLNILELGTGSGCIAISLLCEL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603 132 PDCEITAVDRMPDAVSLAQRNAQNLAIKN-IHILQSDWFSALAGQQFAMIVSNPPYID-EQDPHLQQGDVRFEPLTALVA 209
Cdd:PRK01544 161 PNANVIATDISLDAIEVAKSNAIKYEVTDrIQIIHSNWFENIEKQKFDFIVSNPPYIShSEKSEMAIETINYEPSIALFA 240
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446378603 210 ADSGMADIVHIIEQSRNALVSGGFLLLEHGWQQGEAVRQAFIHAGYHDVETCRDYGDNERV------TLGRYY 276
Cdd:PRK01544 241 EEDGLQAYFIIAENAKQFLKPNGKIILEIGFKQEEAVTQIFLDHGYNIESVYKDLQGHSRVilispiNLNRSY 313
RsmC COG2813
16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
76-236 1.47e-25

16S rRNA G1207 methylase RsmC [Translation, ribosomal structure and biogenesis]; 16S rRNA G1207 methylase RsmC is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 442062 [Multi-domain]  Cd Length: 191  Bit Score: 99.88  E-value: 1.47e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603  76 EFWSLP-LFvSPATLiprpD--TECLVEQALARLPEqpcRILDLGTGTGAIALALASERPDCEITAVDRMPDAVSLAQRN 152
Cdd:COG2813   21 TFVTLPgVF-SRDRL----DigTRLLLEHLPEPLGG---RVLDLGCGYGVIGLALAKRNPEARVTLVDVNARAVELARAN 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603 153 AQNLAIKNIHILQSDWFSALAGQQFAMIVSNPPYideqdpHlQQGDVRFEpltalvaadsgmadIVH-IIEQSRNALVSG 231
Cdd:COG2813   93 AAANGLENVEVLWSDGLSGVPDGSFDLILSNPPF------H-AGRAVDKE--------------VAHaLIADAARHLRPG 151

                 ....*
gi 446378603 232 GFLLL 236
Cdd:COG2813  152 GELWL 156
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
102-186 2.98e-22

tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) A37 N6-methylase TrmN6 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443299 [Multi-domain]  Cd Length: 238  Bit Score: 92.13  E-value: 2.98e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603 102 ALARLPeQPCRILDLGTGTGAIALALASERPDCEITAVDRMPDAVSLAQRNAQNLAIKN-IHILQSD---WFSALAGQQF 177
Cdd:COG4123   31 AFAPVK-KGGRVLDLGTGTGVIALMLAQRSPGARITGVEIQPEAAELARRNVALNGLEDrITVIHGDlkeFAAELPPGSF 109

                 ....*....
gi 446378603 178 AMIVSNPPY 186
Cdd:COG4123  110 DLVVSNPPY 118
MTS pfam05175
Methyltransferase small domain; This domain is found in ribosomal RNA small subunit ...
112-236 8.37e-22

Methyltransferase small domain; This domain is found in ribosomal RNA small subunit methyltransferase C as well as other methyltransferases.


Pssm-ID: 428349 [Multi-domain]  Cd Length: 170  Bit Score: 89.19  E-value: 8.37e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603  112 RILDLGTGTGAIALALASERPDCEITAVDRMPDAVSLAQRNAQNLAIKNIHILQSDWFSALAGQQFAMIVSNPPYideqd 191
Cdd:pfam05175  34 KVLDLGCGAGVLGAALAKESPDAELTMVDINARALESARENLAANGLENGEVVASDVYSGVEDGKFDLIISNPPF----- 108
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 446378603  192 pHlQQGDVRFepltalvaadsgmaDIVH-IIEQSRNALVSGGFLLL 236
Cdd:pfam05175 109 -H-AGLATTY--------------NVAQrFIADAKRHLRPGGELWI 138
PrmC_N pfam17827
PrmC N-terminal domain; This entry corresponds to the N-terminal alpha helical domain of the ...
6-73 2.16e-21

PrmC N-terminal domain; This entry corresponds to the N-terminal alpha helical domain of the HemK protein. HemK is a methyltransferase enzyme that carries out the methylation of the N5 nitrogen of the glutamine found in the conserved GGQ motif of class-1 release factors.


Pssm-ID: 436073 [Multi-domain]  Cd Length: 71  Bit Score: 85.22  E-value: 2.16e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603    6 WLREAISQLQAS--ESPRRDAEILLEHVTGKGRTFILAFGETQLTDEQCQQLDALLTRRRDGEPIAHLTG 73
Cdd:pfam17827   2 ALRWASSRLKEAgiESPRLDAELLLAHVLGLDRTDLLLHPEEELSEEELERFEELLERRAAGEPLQYILG 71
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
112-237 5.80e-17

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 74.39  E-value: 5.80e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603 112 RILDLGTGTGAIALALAsERPDCEITAVDRMPDAVSLAQRNAQNLAIKNIHILQSDWFSAL--AGQQFAMIVSNPPYide 189
Cdd:cd02440    1 RVLDLGCGTGALALALA-SGPGARVTGVDISPVALELARKAAAALLADNVEVLKGDAEELPpeADESFDVIISDPPL--- 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 446378603 190 qdphlqqgdvrfepltalvaaDSGMADIVHIIEQSRNALVSGGFLLLE 237
Cdd:cd02440   77 ---------------------HHLVEDLARFLEEARRLLKPGGVLVLT 103
PRK14967 PRK14967
putative methyltransferase; Provisional
91-238 9.14e-17

putative methyltransferase; Provisional


Pssm-ID: 184931 [Multi-domain]  Cd Length: 223  Bit Score: 77.02  E-value: 9.14e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603  91 PRPDTECLVEqALARLPEQP-CRILDLGTGTGAIALAlASERPDCEITAVDRMPDAVSLAQRNAQnLAIKNIHILQSDWF 169
Cdd:PRK14967  18 PQEDTQLLAD-ALAAEGLGPgRRVLDLCTGSGALAVA-AAAAGAGSVTAVDISRRAVRSARLNAL-LAGVDVDVRRGDWA 94
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446378603 170 SALAGQQFAMIVSNPPYIdeqdPHLQQGDVRFEPLTALVAADSGMADIVHIIEQSRNALVSGGFLLLEH 238
Cdd:PRK14967  95 RAVEFRPFDVVVSNPPYV----PAPPDAPPSRGPARAWDAGPDGRAVLDRLCDAAPALLAPGGSLLLVQ 159
PRK14968 PRK14968
putative methyltransferase; Provisional
91-236 3.51e-15

putative methyltransferase; Provisional


Pssm-ID: 237872 [Multi-domain]  Cd Length: 188  Bit Score: 71.85  E-value: 3.51e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603  91 PRPDTECLVEQALARLPEqpcRILDLGTGTGAIALALASErpDCEITAVDRMPDAVSLAQRNAQNLAIKN--IHILQSDW 168
Cdd:PRK14968   8 PAEDSFLLAENAVDKKGD---RVLEVGTGSGIVAIVAAKN--GKKVVGVDINPYAVECAKCNAKLNNIRNngVEVIRSDL 82
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446378603 169 FSALAGQQFAMIVSNPPYIDEQDPHLQQGDVRFepltALVAADSGMADIVHIIEQSRNALVSGGFLLL 236
Cdd:PRK14968  83 FEPFRGDKFDVILFNPPYLPTEEEEEWDDWLNY----ALSGGKDGREVIDRFLDEVGRYLKPGGRILL 146
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
111-183 8.78e-14

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 67.06  E-value: 8.78e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446378603  111 CRILDLGTGTGAIALALASE-RPDCEITAVDRMPDAVSLAQRNAQNLAIKNIHILQSDWFS---ALAGQQFAMIVSN 183
Cdd:pfam13847   5 MRVLDLGCGTGHLSFELAEElGPNAEVVGIDISEEAIEKARENAQKLGFDNVEFEQGDIEElpeLLEDDKFDVVISN 81
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
109-183 1.52e-12

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 62.15  E-value: 1.52e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446378603 109 QPCRILDLGTGTGAIALALASERPDCEITAVDRMPDAVSLAQRNAQnlaikNIHILQSDWFSALAGQQFAMIVSN 183
Cdd:COG4106    1 PPRRVLDLGCGTGRLTALLAERFPGARVTGVDLSPEMLARARARLP-----NVRFVVADLRDLDPPEPFDLVVSN 70
TrmA COG2265
tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure ...
95-185 5.43e-12

tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family [Translation, ribosomal structure and biogenesis]; tRNA/tmRNA/rRNA uracil-C5-methylase, TrmA/RlmC/RlmD family is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441866 [Multi-domain]  Cd Length: 377  Bit Score: 65.20  E-value: 5.43e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603  95 TECLVEQALARLPEQPC-RILDLGTGTGAIALALAseRPDCEITAVDRMPDAVSLAQRNAQNLAIKNIHILQSDWFSALA 173
Cdd:COG2265  218 AEALYAAALEWLDLTGGeRVLDLYCGVGTFALPLA--RRAKKVIGVEIVPEAVEDARENARLNGLKNVEFVAGDLEEVLP 295
                         90
                 ....*....|....*.
gi 446378603 174 ----GQQFAMIVSNPP 185
Cdd:COG2265  296 ellwGGRPDVVVLDPP 311
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
99-183 2.23e-10

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 56.95  E-value: 2.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603  99 VEQALARLPEQPCRILDLGTGTGAIALALASErpDCEITAVDRMPDAVSLAQRNAQNLaikNIHILQSDWFS-ALAGQQF 177
Cdd:COG2227   14 LAALLARLLPAGGRVLDVGCGTGRLALALARR--GADVTGVDISPEALEIARERAAEL---NVDFVQGDLEDlPLEDGSF 88

                 ....*.
gi 446378603 178 AMIVSN 183
Cdd:COG2227   89 DLVICS 94
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
100-255 2.76e-10

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 57.31  E-value: 2.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603 100 EQALARLPEQPC-RILDLGTGTGAIALALAseRPDCEITAVDRMPDAVSLAQRNAQNLAIkNIHILQSDWFS-ALAGQQF 177
Cdd:COG2226   12 EALLAALGLRPGaRVLDLGCGTGRLALALA--ERGARVTGVDISPEMLELARERAAEAGL-NVEFVVGDAEDlPFPDGSF 88
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446378603 178 AMIVSNppyideqdphlqqgdvrfeplTALVAadsgMADIVHIIEQSRNALVSGG-FLLLEHGWQQGEAVRQAFIHAGY 255
Cdd:COG2226   89 DLVISS---------------------FVLHH----LPDPERALAEIARVLKPGGrLVVVDFSPPDLAELEELLAEAGF 142
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
113-183 9.92e-10

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 54.49  E-value: 9.92e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446378603  113 ILDLGTGTGAIALALAsERPDCEITAVDRMPDAVSLAQRNAQNLAIkNIHILQSDWFS-ALAGQQFAMIVSN 183
Cdd:pfam13649   1 VLDLGCGTGRLTLALA-RRGGARVTGVDLSPEMLERARERAAEAGL-NVEFVQGDAEDlPFPDGSFDLVVSS 70
PRK08287 PRK08287
decarboxylating cobalt-precorrin-6B (C(15))-methyltransferase;
102-165 2.51e-09

decarboxylating cobalt-precorrin-6B (C(15))-methyltransferase;


Pssm-ID: 181354  Cd Length: 187  Bit Score: 55.39  E-value: 2.51e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446378603 102 ALARLPEQPCR-ILDLGTGTGAIALALASERPDCEITAVDRMPDAVSLAQRNAQNLAIKNIHILQ 165
Cdd:PRK08287  23 ALSKLELHRAKhLIDVGAGTGSVSIEAALQFPSLQVTAIERNPDALRLIKENRQRFGCGNIDIIP 87
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
101-183 3.57e-09

SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 55.31  E-value: 3.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603 101 QALARLPEqPCRILDLGTGTGAIALALAsERPDCEITAVDRMPDAVSLAQRNAQNLAIKNIHILQSDW--FSALAGQQFA 178
Cdd:COG0500   19 ALLERLPK-GGRVLDLGCGTGRNLLALA-ARFGGRVIGIDLSPEAIALARARAAKAGLGNVEFLVADLaeLDPLPAESFD 96

                 ....*
gi 446378603 179 MIVSN 183
Cdd:COG0500   97 LVVAF 101
rsmC PRK09489
16S rRNA (guanine(1207)-N(2))-methyltransferase RsmC;
112-234 5.42e-09

16S rRNA (guanine(1207)-N(2))-methyltransferase RsmC;


Pssm-ID: 181902 [Multi-domain]  Cd Length: 342  Bit Score: 56.10  E-value: 5.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603 112 RILDLGTGTGAIALALASERPDCEITAVDRMPDAVSLAQRnaqNLAIKNI--HILQSDWFSALAGqQFAMIVSNPPYIDE 189
Cdd:PRK09489 199 KVLDVGCGAGVLSAVLARHSPKIRLTLSDVSAAALESSRA---TLAANGLegEVFASNVFSDIKG-RFDMIISNPPFHDG 274
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 446378603 190 QDphlqqgdvrfeplTALVAADSgmadivhIIEQSRNALVSGGFL 234
Cdd:PRK09489 275 IQ-------------TSLDAAQT-------LIRGAVRHLNSGGEL 299
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
98-182 1.14e-08

Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 53.01  E-value: 1.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603  98 LVEQALARLPEQP-CRILDLGTGTGAIALALAsERPDCEITAVDRMPDAVSLAQRNAQNLAIKN-IHILQSDWFSALAGQ 175
Cdd:COG2230   39 KLDLILRKLGLKPgMRVLDIGCGWGGLALYLA-RRYGVRVTGVTLSPEQLEYARERAAEAGLADrVEVRLADYRDLPADG 117

                 ....*..
gi 446378603 176 QFAMIVS 182
Cdd:COG2230  118 QFDAIVS 124
COG2263 COG2263
Predicted RNA methylase [General function prediction only];
112-185 1.42e-08

Predicted RNA methylase [General function prediction only];


Pssm-ID: 441864 [Multi-domain]  Cd Length: 199  Bit Score: 53.37  E-value: 1.42e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446378603 112 RILDLGTGTG--AIALALASERpdcEITAVDRMPDAVSLAQRNAQNLAiKNIHILQSDWFSALAGQQFAMIVSNPP 185
Cdd:COG2263   48 TVLDLGCGTGmlAIGAALLGAK---KVVGVDIDPEALEIARENAERLG-VRVDFIRADVTRIPLGGSVDTVVMNPP 119
CobL COG2242
Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part ...
102-174 1.77e-08

Precorrin-6B methylase 2 [Coenzyme transport and metabolism]; Precorrin-6B methylase 2 is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441843 [Multi-domain]  Cd Length: 403  Bit Score: 54.79  E-value: 1.77e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446378603 102 ALARL-PEQPCRILDLGTGTGAIALALASERPDCEITAVDRMPDAVSLAQRNAQNLAIKNIHILQSDWFSALAG 174
Cdd:COG2242  239 TLAKLaLRPGDVLWDIGAGSGSVSIEAARLAPGGRVYAIERDPERAALIRANARRFGVPNVEVVEGEAPEALAD 312
RsmD COG0742
16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA ...
111-275 6.40e-08

16S rRNA G966 N2-methylase RsmD [Translation, ribosomal structure and biogenesis]; 16S rRNA G966 N2-methylase RsmD is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 440505 [Multi-domain]  Cd Length: 183  Bit Score: 51.24  E-value: 6.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603 111 CRILDLGTGTGAIAL-AL---ASerpdcEITAVDRMPDAVSLAQRNAQNL-AIKNIHILQSD---WFSALAGQQFAMIVS 182
Cdd:COG0742   43 ARVLDLFAGSGALGLeALsrgAA-----SVVFVEKDRKAAAVIRKNLEKLgLEDRARVIRGDalrFLKRLAGEPFDLVFL 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603 183 NPPYideqdphlQQGDVrfepltalvaadsgmADIVHIIEQSrNALVSGGFLLLEHGWQQGEAVrqafIHAGYHDVETcR 262
Cdd:COG0742  118 DPPY--------AKGLL---------------EKALELLAEN-GLLAPGGLIVVEHSKREELPE----LPAGLELLKE-R 168
                        170
                 ....*....|...
gi 446378603 263 DYGDNeRVTLGRY 275
Cdd:COG0742  169 KYGDT-RLSFYRR 180
YtxK COG0827
Adenine-specific DNA N6-methylase [Replication, recombination and repair];
93-236 1.58e-07

Adenine-specific DNA N6-methylase [Replication, recombination and repair];


Pssm-ID: 440589 [Multi-domain]  Cd Length: 327  Bit Score: 51.49  E-value: 1.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603  93 PDTECLveqALARLPEQ-----PCRILDLGTGTGAIALALASERPDC-EITAVDRMPDAVSLAQRNAqNLAIKNIHILQS 166
Cdd:COG0827   97 PDAIGL---LIGYLVEKftkkeGLRILDPAVGTGNLLTTVLNQLKKKvNAYGVEVDDLLIRLAAVLA-NLQGHPVELFHQ 172
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446378603 167 DWFSALAGQQFAMIVSNPPYIDEQDphlQQGDVRFEpltalVAADSGMADIVH-IIEQSRNALVSGGFLLL 236
Cdd:COG0827  173 DALQPLLIDPVDVVISDLPVGYYPN---DERAKRFK-----LKADEGHSYAHHlFIEQSLNYLKPGGYLFF 235
Rsm22 COG5459
Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) [Translation, ribosomal ...
93-256 4.63e-07

Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) [Translation, ribosomal structure and biogenesis]; Ribosomal protein RSM22 (predicted mitochondrial rRNA methylase) is part of the Pathway/BioSystem: Archaeal ribosomal proteins


Pssm-ID: 444210 [Multi-domain]  Cd Length: 306  Bit Score: 49.95  E-value: 4.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603  93 PDTECLVEQALARLPE-----QPCRILDLGTGTGAIALALASERPDC-EITAVDRMPDAVSLAQR---NAQNLAIKNIHI 163
Cdd:COG5459   59 PATYAAVRAALAELAEagpdfAPLTVLDVGAGPGTAAWAAADAWPSLlDATLLERSAAALALGRRlarAAANPALETAEW 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603 164 LQSDWFSALAGQQFAMIV-SNppYIDEQDPHLQQGDVRfepltALVAADSGMadiVHIIEQSRNAlvsggflllehGWQQ 242
Cdd:COG5459  139 RLADLAAALPAPPADLVVaSY--VLNELADAARAALVD-----RLWLAPDGA---LLIVEPGTPA-----------GSRR 197
                        170
                 ....*....|....
gi 446378603 243 GEAVRQAFIHAGYH 256
Cdd:COG5459  198 LLAARDRLIAAGAH 211
PrmA COG2264
Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];
97-183 1.20e-06

Ribosomal protein L11 methylase PrmA [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441865 [Multi-domain]  Cd Length: 284  Bit Score: 48.63  E-value: 1.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603  97 CLveQALARLPEQPCRILDLGTGTG--AIALAL--ASerpdcEITAVDRMPDAVSLAQRNAQ-NLAIKNIHILQSDwfsA 171
Cdd:COG2264  138 CL--EALEKLLKPGKTVLDVGCGSGilAIAAAKlgAK-----RVLAVDIDPVAVEAARENAElNGVEDRIEVVLGD---L 207
                         90
                 ....*....|..
gi 446378603 172 LAGQQFAMIVSN 183
Cdd:COG2264  208 LEDGPYDLVVAN 219
TrmR COG4122
tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; ...
101-211 1.94e-06

tRNA 5-hydroxyU34 O-methylase TrmR/YrrM [Translation, ribosomal structure and biogenesis]; tRNA 5-hydroxyU34 O-methylase TrmR/YrrM is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443298  Cd Length: 173  Bit Score: 47.10  E-value: 1.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603 101 QALARLpEQPCRILDLGTGTG--AIALALASeRPDCEITAVDRMPDAVSLAQRNAQNLAI-KNIHILQSD---WFSALAG 174
Cdd:COG4122    9 YLLARL-LGAKRILEIGTGTGysTLWLARAL-PDDGRLTTIEIDPERAAIARENFARAGLaDRIRLILGDaleVLPRLAD 86
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 446378603 175 QQFAMIV------SNPPYIDEQDPHLQQGdvrfepltALVAAD 211
Cdd:COG4122   87 GPFDLVFidadksNYPDYLELALPLLRPG--------GLIVAD 121
PRK07402 PRK07402
precorrin-6Y C5,15-methyltransferase subunit CbiT;
105-165 9.25e-06

precorrin-6Y C5,15-methyltransferase subunit CbiT;


Pssm-ID: 180961  Cd Length: 196  Bit Score: 45.37  E-value: 9.25e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446378603 105 RLPEQPCrILDLGTGTGAIALALASERPDCEITAVDRMPDAVSLAQRNAQNLAIKNIHILQ 165
Cdd:PRK07402  37 RLEPDSV-LWDIGAGTGTIPVEAGLLCPKGRVIAIERDEEVVNLIRRNCDRFGVKNVEVIE 96
Methyltransf_4 pfam02390
Putative methyltransferase; This is a family of putative methyltransferases. The aligned ...
113-193 1.21e-05

Putative methyltransferase; This is a family of putative methyltransferases. The aligned region contains the GXGXG S-AdoMet binding site suggesting a putative methyltransferase activity.


Pssm-ID: 367068  Cd Length: 173  Bit Score: 44.59  E-value: 1.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603  113 ILDLGTGTGAIALALASERPDCEITAVDRMPDAVSLAQRNAQNLAIKNIHILQSD----WFSALAGQQFAMIVSNPPyid 188
Cdd:pfam02390   5 FLEIGCGMGGFLVAMAKANPDKNFIGIEIRVPGVAKALKKIDALGLQNLRILCGNaldvLPNYFPPGSLQKIFINFP--- 81

                  ....*
gi 446378603  189 eqDPH 193
Cdd:pfam02390  82 --DPW 84
RsmG COG0357
16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) [Translation, ...
46-182 1.86e-05

16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) [Translation, ribosomal structure and biogenesis]; 16S rRNA G527 N7-methylase RsmG (former glucose-inhibited division protein B) is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 440126  Cd Length: 211  Bit Score: 44.76  E-value: 1.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603  46 QLTDEQCQQLDAL------------LTRRRDgepiahltgVREFWSLPLFvspatliprpdtECLveQALARLPEQPCRI 113
Cdd:COG0357   15 ELSEEQLEQLEAYlelllkwnkkinLTAIRD---------PEELWERHIL------------DSL--ALLPLLPKEGARV 71
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446378603 114 LDLGTGTG--AIALALAseRPDCEITAVDrmpdavSLA------QRNAQNLAIKNIHILQSDWFSALAGQQFAMIVS 182
Cdd:COG0357   72 LDVGSGAGfpGIPLAIA--RPDLQVTLVD------SLGkkiaflREVVRELGLKNVTVVHGRAEELAPREKFDVVTA 140
prmA PRK00517
50S ribosomal protein L11 methyltransferase;
97-183 2.61e-05

50S ribosomal protein L11 methyltransferase;


Pssm-ID: 234786 [Multi-domain]  Cd Length: 250  Bit Score: 44.37  E-value: 2.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603  97 CLveQALARLPEQPCRILDLGTGTG--AIALAL--ASerpdcEITAVDRMPDAVSLAQRNAQ-NLAIKNIHILQSDwfsa 171
Cdd:PRK00517 109 CL--EALEKLVLPGKTVLDVGCGSGilAIAAAKlgAK-----KVLAVDIDPQAVEAARENAElNGVELNVYLPQGD---- 177
                         90
                 ....*....|..
gi 446378603 172 lagQQFAMIVSN 183
Cdd:PRK00517 178 ---LKADVIVAN 186
Methyltransf_16 pfam10294
Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members ...
109-168 3.29e-05

Lysine methyltransferase; Methyltrans_16 is a lysine methyltransferase. characterized members of this family are protein methyltransferases targetting Lys residues in specific proteins, including calmodulin, VCP, Kin17 and Hsp70 proteins.


Pssm-ID: 313513  Cd Length: 172  Bit Score: 43.47  E-value: 3.29e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446378603  109 QPCRILDLGTGTGAIALALASERPDCEITAVDRmPDAVSLAQRN-AQNLAIKNIHILQSDW 168
Cdd:pfam10294  46 SGLNVLELGSGTGLVGIAVALLLPGASVTITDL-EEALELLKKNiELNALSSKVVVKVLDW 105
RlmL COG0116
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ...
124-186 3.68e-05

23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA G2445 N2-methylase RlmL is part of the Pathway/BioSystem: 23S rRNA modification


Pssm-ID: 439886 [Multi-domain]  Cd Length: 369  Bit Score: 44.32  E-value: 3.68e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446378603 124 ALALASERPDCEITAVDRMPDAVSLAQRNAQNLAI-KNIHILQSDWFSALAGQQFAMIVSNPPY 186
Cdd:COG0116  241 AEARIKRDPPLPIFGSDIDPRAIEAARENAERAGVaDLIEFEQADFRDLEPPAEPGLIITNPPY 304
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
98-196 5.42e-05

Predicted methyltransferase, contains TPR repeat [General function prediction only];


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 42.68  E-value: 5.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603  98 LVEQALARLPEQP-CRILDLGTGTGAIALALAsERPDcEITAVDRMPDAVSLAQRNAQnlaikNIHILQSDwFSALA--G 174
Cdd:COG4976   34 LAEELLARLPPGPfGRVLDLGCGTGLLGEALR-PRGY-RLTGVDLSEEMLAKAREKGV-----YDRLLVAD-LADLAepD 105
                         90       100
                 ....*....|....*....|....
gi 446378603 175 QQFAMIVSN--PPYIDEQDPHLQQ 196
Cdd:COG4976  106 GRFDLIVAAdvLTYLGDLAAVFAG 129
PRK06202 PRK06202
hypothetical protein; Provisional
100-154 6.48e-05

hypothetical protein; Provisional


Pssm-ID: 180466 [Multi-domain]  Cd Length: 232  Bit Score: 43.07  E-value: 6.48e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446378603 100 EQALARLPEQPCRILDLGTGTG--AIALALASERP--DCEITAVDRMPDAVSLAQRNAQ 154
Cdd:PRK06202  51 LLRPALSADRPLTLLDIGCGGGdlAIDLARWARRDglRLEVTAIDPDPRAVAFARANPR 109
pcm PRK00312
protein-L-isoaspartate(D-aspartate) O-methyltransferase;
90-167 6.98e-05

protein-L-isoaspartate(D-aspartate) O-methyltransferase;


Pssm-ID: 178974 [Multi-domain]  Cd Length: 212  Bit Score: 42.88  E-value: 6.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603  90 IPRPDTECLVEQALARLPEQpcRILDLGTGTG---AIaLALASERpdceITAVDRMPDAVSLAQRNAQNLAIKNIHILQS 166
Cdd:PRK00312  61 ISQPYMVARMTELLELKPGD--RVLEIGTGSGyqaAV-LAHLVRR----VFSVERIKTLQWEAKRRLKQLGLHNVSVRHG 133

                 .
gi 446378603 167 D 167
Cdd:PRK00312 134 D 134
TIGR00091 TIGR00091
tRNA (guanine-N(7)-)-methyltransferase; This predicted S-adenosylmethionine-dependent ...
113-167 1.22e-04

tRNA (guanine-N(7)-)-methyltransferase; This predicted S-adenosylmethionine-dependent methyltransferase is found in a single copy in most Bacteria. It is also found, with a short amino-terminal extension in eukaryotes. Its function is unknown. In E. coli, this protein flanks the DNA repair protein MutY, also called micA. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 161703  Cd Length: 194  Bit Score: 41.96  E-value: 1.22e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 446378603  113 ILDLGTGTGAIALALASERPDCEITAVDRMPDAVSLAQRNAQNLAIKNIHILQSD 167
Cdd:TIGR00091  20 HLEIGCGKGRFLIDMAKQNPDKNFLGIEIHTPIVLAANNKANKLGLKNLHVLCGD 74
Cons_hypoth95 pfam03602
Conserved hypothetical protein 95;
109-192 2.68e-04

Conserved hypothetical protein 95;


Pssm-ID: 427391 [Multi-domain]  Cd Length: 179  Bit Score: 40.69  E-value: 2.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603  109 QPCRILDLGTGTGAIALALASeRPDCEITAVDRMPDAVSLAQRNAQNLAIKNIHILQSDW--FSALAGQ--QFAMIVSNP 184
Cdd:pfam03602  41 EGARVLDLFAGSGALGLEALS-RGAKRVTLVEKDKRAVQILKENLQLLGLPGAVLVMDALlaLLRLAGKgpVFDIVFLDP 119

                  ....*...
gi 446378603  185 PYIDEQDP 192
Cdd:pfam03602 120 PYAKGLIE 127
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
114-162 4.79e-04

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 38.41  E-value: 4.79e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 446378603  114 LDLGTGTGAIALALAseRPDCEITAVDRMPDAVSLAQRNAQNLAIKNIH 162
Cdd:pfam08241   1 LDVGCGTGLLTELLA--RLGARVTGVDISPEMLELAREKAPREGLTFVV 47
Trm5 COG2520
tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 ...
112-167 4.88e-04

tRNA G37 N-methylase Trm5 [Translation, ribosomal structure and biogenesis]; tRNA G37 N-methylase Trm5 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442010 [Multi-domain]  Cd Length: 333  Bit Score: 41.00  E-value: 4.88e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446378603 112 RILDLGTGTGAIALALASERPdCEITAVDRMPDAVSLAQRNAQ-NLAIKNIHILQSD 167
Cdd:COG2520  183 RVLDMFAGVGPFSIPIAKRSG-AKVVAIDINPDAVEYLKENIRlNKVEDRVTPILGD 238
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
114-183 7.30e-04

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 38.12  E-value: 7.30e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446378603  114 LDLGTGTGAIALALASERPDCEITAVDRMPDAVSLA-QRNAQN--LAIKNIHILQSDwFSALAGQQFAMIVSN 183
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLEYTGLDISPAALEAArERLAALglLNAVRVELFQLD-LGELDPGSFDVVVAS 72
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
103-183 1.02e-03

malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin biosynthetic gene clusters in proteobacteria, firmicutes, green-sulfur bacteria, fusobacterium and bacteroides, carries out an enzymatic step prior to the formation of pimeloyl-CoA, namely O-methylation of the malonyl group preferentially while on acyl carrier protein. The enzyme is recognizable as a methyltransferase by homology. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273953 [Multi-domain]  Cd Length: 240  Bit Score: 39.58  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603  103 LARLPE----QPCRILDLGTGTGAIALALASERPDCEITAVDRMPdaVSLAQrnAQNLAIKNIHILQSDWFSA-LAGQQF 177
Cdd:TIGR02072  24 LALLKEkgifIPASVLDIGCGTGYLTRALLKRFPQAEFIALDISA--GMLAQ--AKTKLSENVQFICGDAEKLpLEDSSF 99

                  ....*.
gi 446378603  178 AMIVSN 183
Cdd:TIGR02072 100 DLIVSN 105
TehB pfam03848
Tellurite resistance protein TehB;
109-182 1.75e-03

Tellurite resistance protein TehB;


Pssm-ID: 397776  Cd Length: 193  Bit Score: 38.68  E-value: 1.75e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446378603  109 QPCRILDLGTGTGAIALALASERPDceITAVDRMPDAVSLAQRNAQNLAIKNIHILQSDWFSALAGQQFAMIVS 182
Cdd:pfam03848  30 KPGKVLDLGCGQGRNSLYLSLLGYD--VTAWDKNENSIANLQRIKEKENLDNIHTALYDINNATIDENYDFILS 101
RsmA COG0030
16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase ...
112-186 2.53e-03

16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase/AP lyase activity) [Translation, ribosomal structure and biogenesis]; 16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase/AP lyase activity) is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 439801 [Multi-domain]  Cd Length: 270  Bit Score: 38.57  E-value: 2.53e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446378603 112 RILDLGTGTGAIALALAsERPDcEITAVDRMPDAVSLAQRNAQNLaiKNIHILQSD----WFSALAGQQFAMIVSNPPY 186
Cdd:COG0030   40 TVLEIGPGLGALTRALL-ERAA-RVTAVEIDRRLAAILRETFAAY--PNLTVIEGDalkvDLPALAAGEPLKVVGNLPY 114
COG4076 COG4076
Predicted RNA methylase [General function prediction only];
100-167 3.56e-03

Predicted RNA methylase [General function prediction only];


Pssm-ID: 443253 [Multi-domain]  Cd Length: 230  Bit Score: 38.09  E-value: 3.56e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446378603 100 EQALARL--PEQpcRILDLGTGTGAIALaLASERPDCEITAVDRMPDAVSLAQRN-AQNLAIKNIHILQSD 167
Cdd:COG4076   26 KAAIERVvkPGD--VVLDIGTGSGLLSM-LAARAGAKKVYAVEVNPDIAAVARRIiAANGLSDRITVINAD 93
PrmA pfam06325
Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal ...
97-154 4.10e-03

Ribosomal protein L11 methyltransferase (PrmA); This family consists of several Ribosomal protein L11 methyltransferase (EC:2.1.1.-) sequences.


Pssm-ID: 428888 [Multi-domain]  Cd Length: 294  Bit Score: 38.02  E-value: 4.10e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446378603   97 CLveQALARLPEQPCRILDLGTGTG--AIALAL--ASerpdcEITAVDRMPDAVSLAQRNAQ 154
Cdd:pfam06325 151 CL--EALERLVKPGESVLDVGCGSGilAIAALKlgAK-----KVVGVDIDPVAVRAAKENAE 205
PRK08317 PRK08317
hypothetical protein; Provisional
92-158 4.23e-03

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 37.61  E-value: 4.23e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603  92 RPDTECLVEQALARLPEQPC-RILDLGTGTGAIALALASE-RPDCEITAVDRMPDAVSLAQ-RNAQNLAI 158
Cdd:PRK08317   1 LPDFRRYRARTFELLAVQPGdRVLDVGCGPGNDARELARRvGPEGRVVGIDRSEAMLALAKeRAAGLGPN 70
PRK11207 PRK11207
tellurite resistance methyltransferase TehB;
92-182 5.17e-03

tellurite resistance methyltransferase TehB;


Pssm-ID: 183040  Cd Length: 197  Bit Score: 37.02  E-value: 5.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603  92 RPDTEclVEQALARLPeqPCRILDLGTGTGAIALALASERPDceITAVDRMPDAVSLAQRNAQNLAIKNIHILQSDWFSA 171
Cdd:PRK11207  17 RTHSE--VLEAVKVVK--PGKTLDLGCGNGRNSLYLAANGFD--VTAWDKNPMSIANLERIKAAENLDNLHTAVVDLNNL 90
                         90
                 ....*....|.
gi 446378603 172 LAGQQFAMIVS 182
Cdd:PRK11207  91 TFDGEYDFILS 101
PRK11036 PRK11036
tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;
100-166 5.54e-03

tRNA uridine 5-oxyacetic acid(34) methyltransferase CmoM;


Pssm-ID: 182918  Cd Length: 255  Bit Score: 37.64  E-value: 5.54e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446378603 100 EQALARLPEQPCRILDLGTGTGAIALALAsERPDcEITAVDRMPDAVSLAQRNAQ-NLAIKNIHILQS 166
Cdd:PRK11036  35 DRLLAELPPRPLRVLDAGGGEGQTAIKLA-ELGH-QVILCDLSAEMIQRAKQAAEaKGVSDNMQFIHC 100
HsdM COG0286
Type I restriction-modification system, DNA methylase subunit [Defense mechanisms];
91-261 5.99e-03

Type I restriction-modification system, DNA methylase subunit [Defense mechanisms];


Pssm-ID: 440055 [Multi-domain]  Cd Length: 243  Bit Score: 37.09  E-value: 5.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603  91 PRPDTECLVEQALarlPEQPCRILDLGTGTGAIALALA--------SERPDCEITAVDRMPDAVSLAqrnAQNLAIKNI- 161
Cdd:COG0286   28 PREVVRLMVELLD---PKPGETVYDPACGSGGFLVEAAeylkehggDERKKLSLYGQEINPTTYRLA---KMNLLLHGIg 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603 162 --HILQSDWFSALAGQ--QFAMIVSNPPYIDEQDPHLQQGDV--RFEPLTALVaADSGMADIVHIIEQ----SRNALV-S 230
Cdd:COG0286  102 dpNIELGDTLSNDGDEleKFDVVLANPPFGGKWKKEELKDDLlgRFGYGLPPK-SNADLLFLQHILSLlkpgGRAAVVlP 180
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 446378603 231 GGFL-----------LLEHGWQqgEAV----RQAFIHAGyhdVETC 261
Cdd:COG0286  181 DGVLfrgaekeirkkLLENDLL--EAIiglpSNLFYNTG---IPTC 221
PRK07580 PRK07580
Mg-protoporphyrin IX methyl transferase; Validated
99-154 8.27e-03

Mg-protoporphyrin IX methyl transferase; Validated


Pssm-ID: 236059 [Multi-domain]  Cd Length: 230  Bit Score: 36.74  E-value: 8.27e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603  99 VEQALARLPEQP----CRILDLGTGTGAIALALAseRPDCEITAVDRMPDAVSLAQRNAQ 154
Cdd:PRK07580  49 RDTVLSWLPADGdltgLRILDAGCGVGSLSIPLA--RRGAKVVASDISPQMVEEARERAP 106
PRK14904 PRK14904
16S rRNA methyltransferase B; Provisional
101-185 8.58e-03

16S rRNA methyltransferase B; Provisional


Pssm-ID: 237858 [Multi-domain]  Cd Length: 445  Bit Score: 37.35  E-value: 8.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446378603 101 QALARL---PEQPCRILDLGTGTGAIALALASERPDC-EITAVDRMPDAVSLAQRNAQNLAIKNIHILQSDWFSALAGQQ 176
Cdd:PRK14904 239 QALACLllnPQPGSTVLDLCAAPGGKSTFMAELMQNRgQITAVDRYPQKLEKIRSHASALGITIIETIEGDARSFSPEEQ 318

                 ....*....
gi 446378603 177 FAMIVSNPP 185
Cdd:PRK14904 319 PDAILLDAP 327
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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